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Lysyl oxidase from jumbo squid ( Dosidicus gigas ) muscle: detection and partial purification
Author(s) -
TorresArreola Wilfrido,
EzquerraBrauer Josafat M.,
FigueroaSoto Ciria G.,
ValenzuelaSoto Elisa M.,
GarciaSanchez Guillermina,
MarquezRios Enrique,
PachecoAguilar Ramón
Publication year - 2011
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2011.02676.x
Subject(s) - sephadex , lysyl oxidase , chemistry , chromatography , squid , biochemistry , urea , yield (engineering) , size exclusion chromatography , extraction (chemistry) , enzyme , biology , fishery , materials science , metallurgy
Summary Lysyl oxidase (LOX) was detected and partially purified from jumbo squid ( Dosidicus gigas ) muscle, for the first time. A procedure for the purification of LOX from jumbo squid muscle which consisted of urea extraction, Sephadex G‐75 and anion exchange chromatography was developed. Activity of partially purified LOX was 390‐fold higher than the original extract. Two protein fractions with 32 and 24 kDa were detected by SDS‐PAGE. The enzyme was strongly inhibited by β‐aminopropionitrile fumarate, a specific LOX inhibitor. LOX was purified with 3.8% yield, showing a specific activity of 0.078 IU mg −1 protein. This knowledge will help understand the behaviour of jumbo squid protein during cool storage or manufacture.